ReviewBiophysical chemistry2016
Cold denaturation as a tool to measure protein stability.
Review in Biophysical chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
33 citing papers in PubMed.
- Impact of single freeze-thaw cycles on human serum proteins: Implications for mass spectrometry biomarker validation.iScience · 2026Article
- Modification of Muscle Proteins Induced by Novel Non-Thermal Processing: Theory, Characterization, and Consequences.Foods (Basel, Switzerland) · 2026Review
- Proteome-wide identification of metamorphic protein candidates using mass spectrometry.bioRxiv : the preprint server for biology · 2025Article
- Potassium binding by carbonyl clusters, halophilic adaptation and catalysis of Haloferax mediterranei D-2-hydroxyacid dehydrogenase.Communications biology · 2025Article
- Interplay of protein fluctuation and associated water dynamics in osmolyte-induced stabilization.Biophysical journal · 2025Article
- Direct Detection of Bound Water in Hydrated Powders of Lysozyme by Differential Scanning Calorimetry.ACS physical chemistry Au · 2024Article
- High-throughput system for the thermostability analysis of proteins.Protein science : a publication of the Protein Society · 2024Article
- Engineered ice-binding protein (FfIBP) shows increased stability and resistance to thermal and chemical denaturation compared to the wildtype.Scientific reports · 2024Article
- Article
- Helping proteins come in from the cold: 5 burning questions about cold-active enzymes.BBA advances · 2024Review
- Protein Stability─Analysis of Heat and Cold Denaturation without and with Unfolding Models.The journal of physical chemistry. B · 2023Article
- Salt-Specific Suppression of the Cold Denaturation of Thermophilic Multidomain Initiation Factor 2.International journal of molecular sciences · 2023Article
- Impact of temperature on optical sensing in biology based on investigation of SARS-CoV-2.Journal of biophotonics · 2023Article
- Thermofluor-Based Optimization Strategy for the Stabilization of Recombinant Human Soluble Catechol-International journal of molecular sciences · 2022Article
- Conformational Stability and Denaturation Processes of Proteins Investigated by Electrophoresis under Extreme Conditions.Molecules (Basel, Switzerland) · 2022Review
- Cold Denaturation of Proteins in the Absence of Solvent: Implications for Protein Storage.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2022Article
- Cold Denaturation of Proteins in the Absence of Solvent: Implications for Protein Storage.Angewandte Chemie (International ed. in English) · 2022Article
- Molecular understanding of calorimetric protein unfolding experiments.Biophysical reports · 2022Article
- Protein Mutations and Stability, a Link with Disease: The Case Study of Frataxin.Biomedicines · 2022Review
- Functional implication of heat shock protein 70/90 and tubulin in cold stress of Dermacentor silvarum.Parasites & vectors · 2021Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Protein stability is an important issue for the interpretation of a wide variety of biological problems but its assessment is at times difficult. The most common parameter employed to describe protein stability is the temperature of melting, at which the populations of folded and unfolded species are identical. This parameter may yield ambiguous results. It would always be preferable to measure the whole stability curve. The calculation of this curve is greatly facilitated whenever it is possible to observe cold denaturation. Using Yfh1, one of the few proteins whose cold denaturation occurs at neutral pH and low ionic strength, we could measure the variation of its full stability curve under several environmental conditions. Here we show the advantages of gauging stability as a function of external variables using stability curves.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.